ABC transporter architecture and mechanism: implications from the crystal structures of BtuCD and BtuF

FEBS Lett. 2004 Apr 30;564(3):264-8. doi: 10.1016/S0014-5793(04)00289-3.

Abstract

ABC transporters are ubiquitous membrane proteins that facilitate unidirectional substrate translocation across the lipid bilayer. Over the past five years, new crystal structures have advanced our understanding of how ABC transporters couple adenosine triphosphate (ATP) hydrolysis to substrate transport. In the following, we will briefly review the results of these structural investigations and outline their mechanistic implications.

Publication types

  • Review

MeSH terms

  • ATP-Binding Cassette Transporters / chemistry*
  • ATP-Binding Cassette Transporters / metabolism
  • Adenosine Triphosphate / metabolism
  • Crystallography, X-Ray
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism
  • Models, Molecular
  • Periplasmic Binding Proteins / chemistry*
  • Periplasmic Binding Proteins / metabolism
  • Protein Conformation*

Substances

  • ATP-Binding Cassette Transporters
  • BtuC peptide, E coli
  • Escherichia coli Proteins
  • Periplasmic Binding Proteins
  • btuF protein, E coli
  • Adenosine Triphosphate